Results 311 to 320 of about 153,000 (334)
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The Journal of Biochemistry, 1968
1. A method for isolation of troponin from native tropomyosin was described. 2. Troponin in combination with tropomyosin restored the whole activity of native tropomyosin in sensitizing the interaction of myosin and actin to Ca ion. 3. Troponin was found to bind nearly 4 moles of Ca per 10 5 g, of which most were exchangeable.
Fumiko Ebashi +2 more
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1. A method for isolation of troponin from native tropomyosin was described. 2. Troponin in combination with tropomyosin restored the whole activity of native tropomyosin in sensitizing the interaction of myosin and actin to Ca ion. 3. Troponin was found to bind nearly 4 moles of Ca per 10 5 g, of which most were exchangeable.
Fumiko Ebashi +2 more
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The binding sites of rabbit skeletal troponin-I on troponin-T
Canadian Journal of Biochemistry, 1980Various fragments derived from rabbit skeletal muscle troponin-T (Tn-T) by chemical and (or) proteolytic cleavage were mixed with whole troponin-I (Tn-I) and applied to a Sephadex G-75 gel filtration column in order to determine the binding site of Tn-I on Tn-T. This site of interaction was found to span two distinct regions of Tn-T.
Joyce R. Pearlstone, Lawrence B. Smillie
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Defining the Region of Troponin-I that Binds to Troponin-C
Biochemistry, 1999The kinetics and energetics of the binding of three troponin-I peptides, corresponding to regions 96-131 (TnI96-131), 96-139 (TnI96-139), and 96-148 (TnI96-148), to skeletal chicken troponin-C were investigated using multinuclear, multidimensional NMR spectroscopy.
Ryan T. McKay +4 more
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Comparison of troponin-I and troponin-T after pediatric cardiovascular operation [PDF]
The Annals of Thoracic Surgery, 1998 Although the diagnostic value of troponin-T in childhood is documented, little is known about the significance of troponin-I. It was the aim of this study to compare the diagnostic value of troponin-I and troponin-T in children and newborns to assess the perioperative potential myocardial damage.Forty-eight children, mean, 51+/-54 months (mean value +/-
Thierry Carrel +5 more
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Interactions among Chymotryptic Troponin T Subfragments, Tropomyosin, Troponin I and Troponin C1
The Journal of Biochemistry, 1984The binding of various combinations of chymotryptic troponin T subfragments, troponin I and troponin C to tropomyosin, troponin C and troponin I was examined semiquantitatively by using affinity chromatography. The interaction between troponin T2 and troponin I intensified the interaction between troponin T2 (or troponin T) and tropomyosin.
Iwao Ohtsuki, Masaru Tanokura
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Biochemistry, 2000
Troponin I (TnI) is the component of the troponin complex, TnI, TnC, TnT, that is responsible for inhibition of actomyosin ATPase activity. Using the fluorescence of pyrene-labeled tropomyosin (Tm), we probed the interaction of TnI and TnIC with Tm on the reconstituted muscle thin filament.
X Zhou, E P Morris, Sherwin S. Lehrer
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Troponin I (TnI) is the component of the troponin complex, TnI, TnC, TnT, that is responsible for inhibition of actomyosin ATPase activity. Using the fluorescence of pyrene-labeled tropomyosin (Tm), we probed the interaction of TnI and TnIC with Tm on the reconstituted muscle thin filament.
X Zhou, E P Morris, Sherwin S. Lehrer
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Biochemistry, 2001
Multidimensional heteronuclear magnetic resonance studies of the cardiac troponin C/troponin I(1-80)/troponin I(129-166) complex demonstrated that cardiac troponin I(129-166), corresponding to the adjacent inhibitory and regulatory regions, interacts with and induces an opening of the cardiac troponin C regulatory domain.
Herbert C. Cheung +6 more
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Multidimensional heteronuclear magnetic resonance studies of the cardiac troponin C/troponin I(1-80)/troponin I(129-166) complex demonstrated that cardiac troponin I(129-166), corresponding to the adjacent inhibitory and regulatory regions, interacts with and induces an opening of the cardiac troponin C regulatory domain.
Herbert C. Cheung +6 more
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Troponin I: Inhibitor or facilitator
Molecular and Cellular Biochemistry, 1999TN-I occurs as a homologous group of proteins which form part of the regulatory system of vertebrate and invertebrate striated muscle. These proteins are present in vertebrate muscle as isoforms, Mr 21000-24000, that are specific for the muscle type and under individual genetic control.
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Structural and functional studies on Troponin I and Troponin C interactions
Journal of Cellular Biochemistry, 2001AbstractTroponin I (TnI) peptides (TnI inhibitory peptide residues 104–115, Ip; TnI regulatory peptide resides 1–30, TnI1–30), recombinant Troponin C (TnC) and Troponin I mutants were used to study the structural and functional relationship between TnI and TnC.
S M, Ngai +5 more
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Skeletal troponin I cross-reactivity in different cardiac troponin I assay versions
Clinical Biochemistry, 2015To study the skeletal troponin I (skTnI) cross-reactivity of four different commercially available antibodies in four cardiac troponin I (cTnI) research assay versions having the same epitope specificity as evidenced by peptide mapping.The four research assays all use two solid phase antibodies and one detection antibody attached to intrinsically ...
Tarja Puolakanaho +5 more
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